MolNFT v1 · #151514 · protein

Structure of eal enzyme BD1971 - camp bound form

6HQ4: “Structure of eal enzyme BD1971 - camp bound form”. X-ray diffraction, 2 ligands (CMP, MG), 10 pockets (best druggability 0.67). MolNFT v1 #151514 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6HQ4
Type: protein
Length: 742 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Eal enzyme BD1971
UniProt: Q6MLN6
Ligands: CMP, MG
Pockets: 10 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Eal enzyme BD1971	protein	374	42% helix, 25% strand	Q6MLN6
B	Eal enzyme BD1971	protein	368	43% helix, 26% strand	Q6MLN6

Ligands and binding sites

CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	465	0.67	0.79	45	MG
2	150	0.66	0.87	23	CMP
3	522	0.66	0.77	56	empty
4	184	0.66	0.85	27	CMP
5	58	0.51	0.86	13	empty

Interfaces

1 interface between chains.

A–B · 3001 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

6HQ4 · Structure of EAL enzyme Bd1971 - cAMP bound form · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q6MLN6
Elsewhere: RCSB PDB 6HQ4 · PDBe 6HQ4 · UniProt Q6MLN6

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.